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- W1991006838 abstract "Thimet oligopeptidase (EC 3.4.24.15; TOP) is a Zn(II) endopeptidase implicated in physiological regulation of processes involving neuropeptides. The present study clarifies the active site structure and mechanism of catalysis of TOP. The enzyme exhibited a bell-shaped pH dependence of activity having an acidic limb due to a protonation event with a pK(a) of 5.7 and a basic limb with pK(a) of 8.8. The acidic limb can be attributed to protonation of a residue affecting k(cat) while the alkaline limb may be due to conformational change. Mutation of Tyr612 to Phe resulted in more than 400-fold decrease in activity. This result, supported by modeling studies, implicates Tyr612 in transition state stabilization analogous to the role of His231 of thermolysin." @default.
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- W1991006838 date "2003-05-24" @default.
- W1991006838 modified "2023-09-27" @default.
- W1991006838 title "pH dependence studies provide insight into the structure and mechanism of thimet oligopeptidase (EC 3.4.24.15)" @default.
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- W1991006838 doi "https://doi.org/10.1016/s0014-5793(03)00548-9" @default.
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